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P03188

- GB_EBVB9

UniProt

P03188 - GB_EBVB9

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Protein

Envelope glycoprotein B

Gene

gB

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Envelope glycoprotein that forms spikes at the surface of virion envelope. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding of gp350/220 to its receptor, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei432 – 4332Cleavage; by host furinSequence Analysis

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein B
Short name:
gB
Alternative name(s):
GP115
Glycoprotein GP110
Gene namesi
Name:gB
ORF Names:BALF4
OrganismiEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Taxonomic identifieri10377 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007640: Genome

Subcellular locationi

Virion membrane By similarity; Single-pass type I membrane protein By similarity. Host cell membrane By similarity; Single-pass type I membrane protein By similarity. Host endosome membrane By similarity; Single-pass type I membrane protein By similarity. Host Golgi apparatus membrane By similarity; Single-pass type I membrane protein By similarity
Note: During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 732710Virion surfaceSequence AnalysisAdd
BLAST
Transmembranei733 – 75321HelicalSequence AnalysisAdd
BLAST
Topological domaini754 – 857104IntravirionSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell endosome Source: UniProtKB-KW
  2. host cell Golgi apparatus Source: UniProtKB-KW
  3. host cell plasma membrane Source: UniProtKB-KW
  4. integral component of membrane Source: UniProtKB-KW
  5. viral envelope Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host endosome, Host Golgi apparatus, Host membrane, Membrane, Viral envelope protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi112 – 1132WY → HR: Loss of fusion with epithelial cells. 1 Publication
Mutagenesisi193 – 1964WLIW → RVEA: Loss of fusion with epithelial cells. 1 Publication
Mutagenesisi428 – 4325RRRRR → DDDDK: Complete loss of proteolytic cleavage. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 857835Envelope glycoprotein BPRO_0000038190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 528
Disulfide bondi68 ↔ 484
Glycosylationi76 – 761N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi141 ↔ 206
Glycosylationi163 – 1631N-linked (GlcNAc...); by host1 Publication
Glycosylationi290 – 2901N-linked (GlcNAc...); by host1 Publication
Disulfide bondi295 ↔ 342
Glycosylationi329 – 3291N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi348 – 3481N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi395 – 3951N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi436 – 4361N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi551 ↔ 588By similarity
Glycosylationi563 – 5631N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi629 – 6291N-linked (GlcNAc...); by host1 Publication

Post-translational modificationi

A proteolytic cleavage by host furin generates two subunits that remain linked by disulfide bonds.3 Publications

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotrimer; disulfide-linked.By similarity

Protein-protein interaction databases

DIPiDIP-47669N.
MINTiMINT-6768112.

Structurei

Secondary structure

1
857
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi58 – 603Combined sources
Beta strandi77 – 8711Combined sources
Beta strandi92 – 11019Combined sources
Beta strandi115 – 12511Combined sources
Helixi129 – 1357Combined sources
Turni136 – 1383Combined sources
Beta strandi140 – 14910Combined sources
Beta strandi152 – 1576Combined sources
Helixi158 – 1603Combined sources
Beta strandi165 – 1673Combined sources
Beta strandi179 – 1835Combined sources
Beta strandi197 – 21519Combined sources
Beta strandi222 – 2243Combined sources
Beta strandi229 – 2324Combined sources
Turni248 – 2503Combined sources
Beta strandi251 – 2577Combined sources
Helixi262 – 2643Combined sources
Beta strandi272 – 2787Combined sources
Beta strandi283 – 2875Combined sources
Helixi291 – 2933Combined sources
Beta strandi296 – 31015Combined sources
Beta strandi315 – 3195Combined sources
Turni320 – 3234Combined sources
Beta strandi324 – 3296Combined sources
Helixi341 – 3433Combined sources
Helixi344 – 35613Combined sources
Turni357 – 3615Combined sources
Beta strandi362 – 3687Combined sources
Beta strandi370 – 3745Combined sources
Beta strandi379 – 3879Combined sources
Helixi458 – 49841Combined sources
Helixi502 – 5109Combined sources
Beta strandi516 – 5194Combined sources
Beta strandi522 – 5254Combined sources
Beta strandi533 – 5386Combined sources
Beta strandi556 – 5605Combined sources
Beta strandi567 – 5726Combined sources
Beta strandi576 – 5794Combined sources
Beta strandi593 – 5986Combined sources
Beta strandi601 – 6066Combined sources
Beta strandi609 – 6157Combined sources
Turni616 – 6183Combined sources
Helixi646 – 6505Combined sources
Helixi657 – 67317Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FVCX-ray3.20A23-685[»]
ProteinModelPortaliP03188.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03188.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni111 – 1144Involved in fusion and/or binding to host membraneSequence Analysis
Regioni193 – 1975Involved in fusion and/or binding to host membraneSequence Analysis
Regioni561 – 62060OligomerizationAdd
BLAST
Regioni709 – 72921Hydrophobic membrane proximal regionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi428 – 4325Poly-Arg
Compositional biasi836 – 8394Poly-Arg

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR000234. Herpes_Glycoprot_B.
[Graphical view]
PfamiPF00606. Glycoprotein_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03188-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTRRRVLSVV VLLAALACRL GAQTPEQPAP PATTVQPTAT RQQTSFPFRV
60 70 80 90 100
CELSSHGDLF RFSSDIQCPS FGTRENHTEG LLMVFKDNII PYSFKVRSYT
110 120 130 140 150
KIVTNILIYN GWYADSVTNR HEEKFSVDSY ETDQMDTIYQ CYNAVKMTKD
160 170 180 190 200
GLTRVYVDRD GVNITVNLKP TGGLANGVRR YASQTELYDA PGWLIWTYRT
210 220 230 240 250
RTTVNCLITD MMAKSNSPFD FFVTTTGQTV EMSPFYDGKN KETFHERADS
260 270 280 290 300
FHVRTNYKIV DYDNRGTNPQ GERRAFLDKG TYTLSWKLEN RTAYCPLQHW
310 320 330 340 350
QTFDSTIATE TGKSIHFVTD EGTSSFVTNT TVGIELPDAF KCIEEQVNKT
360 370 380 390 400
MHEKYEAVQD RYTKGQEAIT YFITSGGLLL AWLPLTPRSL ATVKNLTELT
410 420 430 440 450
TPTSSPPSSP SPPAPSAARG STPAAVLRRR RRDAGNATTP VPPTAPGKSL
460 470 480 490 500
GTLNNPATVQ IQFAYDSLRR QINRMLGDLA RAWCLEQKRQ NMVLRELTKI
510 520 530 540 550
NPTTVMSSIY GKAVAAKRLG DVISVSQCVP VNQATVTLRK SMRVPGSETM
560 570 580 590 600
CYSRPLVSFS FINDTKTYEG QLGTDNEIFL TKKMTEVCQA TSQYYFQSGN
610 620 630 640 650
EIHVYNDYHH FKTIELDGIA TLQTFISLNT SLIENIDFAS LELYSRDEQR
660 670 680 690 700
ASNVFDLEGI FREYNFQAQN IAGLRKDLDN AVSNGRNQFV DGLGELMDSL
710 720 730 740 750
GSVGQSITNL VSTVGGLFSS LVSGFISFFK NPFGGMLILV LVAGVVILVI
760 770 780 790 800
SLTRRTRQMS QQPVQMLYPG IDELAQQHAS GEGPGINPIS KTELQAIMLA
810 820 830 840 850
LHEQNQEQKR AAQRAAGPSV ASRALQAARD RFPGLRRRRY HDPETAAALL

GEAETEF
Length:857
Mass (Da):95,639
Last modified:July 21, 1986 - v1
Checksum:iD9BCE9487D8A1411
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24806.1.
AJ507799 Genomic DNA. Translation: CAD53463.1.
PIRiA03749. QQBE1L.
RefSeqiYP_401713.1. NC_007605.1.

Genome annotation databases

GeneIDi3783680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24806.1 .
AJ507799 Genomic DNA. Translation: CAD53463.1 .
PIRi A03749. QQBE1L.
RefSeqi YP_401713.1. NC_007605.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3FVC X-ray 3.20 A 23-685 [» ]
ProteinModelPortali P03188.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-47669N.
MINTi MINT-6768112.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3783680.

Miscellaneous databases

EvolutionaryTracei P03188.

Family and domain databases

InterProi IPR000234. Herpes_Glycoprot_B.
[Graphical view ]
Pfami PF00606. Glycoprotein_B. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of the 17,166 base-pair EcoRI fragment C of B95-8 Epstein-Barr virus."
    Bankier A.T., Deininger P.L., Farrell P.J., Barrell B.G.
    Mol. Biol. Med. 1:21-45(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB."
    Gong M., Ooka T., Matsuo T., Kieff E.
    J. Virol. 61:499-508(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROTEIN.
  4. Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
  5. "Characterization of EBV gB indicates properties of both class I and class II viral fusion proteins."
    Backovic M., Leser G.P., Lamb R.A., Longnecker R., Jardetzky T.S.
    Virology 368:102-113(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 112-TRP-TYR-113; 193-TRP--TRP-196 AND 428-ARG--ARG-432, PROTEOLYTIC CLEAVAGE.
  6. "Analysis of Epstein-Barr virus glycoprotein B functional domains via linker insertion mutagenesis."
    Reimer J.J., Backovic M., Deshpande C.G., Jardetzky T., Longnecker R.
    J. Virol. 83:734-747(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: OLIGOMERIZATION REGION.
  7. "Cleavage of Epstein-Barr virus glycoprotein B is required for full function in cell-cell fusion with both epithelial and B cells."
    Sorem J., Longnecker R.
    J. Gen. Virol. 90:591-595(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC CLEAVAGE BY HOST FURIN.
  8. "Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B."
    Backovic M., Longnecker R., Jardetzky T.S.
    Proc. Natl. Acad. Sci. U.S.A. 106:2880-2885(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 23-685, GLYCOSYLATION AT ASN-163; ASN-290 AND ASN-629.

Entry informationi

Entry nameiGB_EBVB9
AccessioniPrimary (citable) accession number: P03188
Secondary accession number(s): Q777B0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 26, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3